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The major human rhinovirus receptor is ICAM-1
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scholarly article
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title
The major human rhinovirus receptor is ICAM-1
(English)
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main subject
virology
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Intercellular adhesion molecule 1
1 reference
stated in
GOA release 2020-03-11
receptor-mediated virion attachment to host cell
1 reference
stated in
GOA release 2020-03-11
author
Alan McClelland
1 reference
stated in
ORCID Public Data File 2021
author name string
J M Greve
series ordinal
1
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G Davis
series ordinal
2
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A M Meyer
series ordinal
3
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C P Forte
series ordinal
4
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S C Yost
series ordinal
5
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C W Marlor
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6
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M E Kamarck
series ordinal
7
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A McClelland
series ordinal
8
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language of work or name
English
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publication date
10 March 1989
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published in
Cell
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volume
56
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page(s)
839-47
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issue
5
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cites work
Monoclonal antibodies which alter the morphology of cultured chick myogenic cells
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Crossref
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Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
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Somatic cell hybrid mapping panels
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How signal sequences maintain cleavage specificity
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Receptor affinities as major determinants of enterovirus tissue tropisms in humans
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Crossref
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Irreversible eclipse of poliovirus by HeLa cells
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reference URL
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Picornavirus receptors and picornavirus multiplication in human-mouse hybrid cell lines
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Crossref
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A collaborative report: rhinoviruses--extension of the numbering system from 89 to 100
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Conservation of the putative receptor attachment site in picornaviruses
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9 Monoclonal antibodies against HLA products and their use in immunoaffinity purification
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Molecular cloning of receptor genes by transfection
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Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1)
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Crossref
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Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families
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Crossref
reference URL
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Monoclonal antibodies which block cellular receptors of poliovirus
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Crossref
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The poliovirus sensitivity (PVS) gene is on chromosome 19q12----q13.2.
1 reference
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Crossref
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Unrelated animal viruses share receptors
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Antibodies to major histocompatibility antigens produced by hybrid cell lines
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Structure of a human common cold virus and functional relationship to other picornaviruses
1 reference
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Myristylation of picornavirus capsid protein VP4 and its structural significance
1 reference
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ICAM, an adhesion ligand of LFA-1, is homologous to the neural cell adhesion molecule NCAM.
1 reference
stated in
Crossref
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Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
1 reference
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Externally disposed plasma membrane proteins. I. Enzymatic iodination of mouse L cells
1 reference
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Southern analysis of genomic DNA with unique and degenerate oligonucleotide probes: a method for reducing probe degeneracy
1 reference
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The complete nucleotide sequence of a common cold virus: human rhinovlrus 14
1 reference
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Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region.
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Sequential steps in attachment of human rhinovirus type 2 to HeLa cells
1 reference
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Crossref
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Production of a monoclonal antibody against an epitope on HeLa cells that is the functional poliovirus binding site
1 reference
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Crossref
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Patterns of amino acids near signal-sequence cleavage sites
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Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase
1 reference
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Three-dimensional structure of poliovirus at 2.9 A resolution.
1 reference
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Crossref
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The atomic structure of Mengo virus at 3.0 A resolution
1 reference
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7 January 2021
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Isolation of a monoclonal antibody that blocks attachment of the major group of human rhinoviruses
1 reference
stated in
Crossref
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https://api.crossref.org/works/10.1016%2F0092-8674%2889%2990688-0
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Characterization of human rhinoviruses displaced by an anti-receptor monoclonal antibody
1 reference
stated in
Crossref
reference URL
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inferred from DOI database lookup
Identifiers
DOI
10.1016/0092-8674(89)90688-0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1683030
OpenCitations bibliographic resource ID
1683030
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1683030
PubMed ID
2538243
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1683030
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